Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain

• DOI: 10.1038/363038a0
• Publication Date: 2003-08-12T00:26:34Z
• Authors: Adrian R. Ferré-D...; George C. Prender...; Edward B. Ziff; Stephen K. Burley
• Keywords: Models, Molecular; Leucine Zippers; 0303 health sciences; Base Sequence; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; Macromolecular Substances; Molecular Sequence Data; DNA; DNA-Binding Proteins; Proto-Oncogene Proteins c-myc; Mice; 03 medical and health sciences; Basic-Leucine Zipper Transcription Factors; X-Ray Diffraction; Escherichia coli; Animals; Nucleic Acid Conformation; Computer Simulation; Amino Acid Sequence; Cloning, Molecular; Protein Binding; Transcription Factors

The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.